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Significance In plants, the retromer complex (VPS35, VPS29, VPS26) has been implicated in retrograde traffic from the endosomes back to thetrans -Golgi network. Nevertheless, vps35 mutants exhibit impaired anterograde traffic toward the vacuole (synthetic, endocytic, and autophagic). This paradox remains an open question. We show that the small molecule endosidin17 (ES17) targets VPS35, which disrupts its association with RABG3f. This, in turn, impairs retromer complex membrane anchoring, producing vps35 mutant-like phenotypes. Using ES17, we found that VPS35–RABG3f binding precedes the release of RABG3f–GTP to interact with the vacuolar homotypic fusion and vacuole protein sorting (HOPS) complex, which is required for fusion of late compartments with the tonoplast. Thus, VPS35–RABG3f interaction constitutes a checkpoint before proceeding with membrane fusion.

Interaction between VPS35 and RABG3f is necessary as a checkpoint to control fusion of late compartments with the vacuole